Structure and dynamics of the type III secretion system
| Project/Area Number |
15H02386
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| Research Category |
Grant-in-Aid for Scientific Research (A)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Structural biochemistry
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| Research Institution | Osaka University |
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Principal Investigator |
Imada Katsumi 大阪大学, 理学研究科, 教授 (40346143)
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| Co-Investigator(Kenkyū-buntansha) |
川岸 郁朗 法政大学, 生命科学部, 教授 (80234037)
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| Co-Investigator(Renkei-kenkyūsha) |
MINAMINO Tohru 大阪大学, 大学院生命機能研究科, 准教授 (20402993)
KAWAMOTO Akihiro 大阪大学, 大学院生命機能研究科, 研究員 (90631523)
KAWAGUCHI Tatsuya 大阪大学, 大学院理学研究科, 助教 (10314353)
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| Project Period (FY) |
2015-04-01 – 2018-03-31
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| Project Status |
Completed (Fiscal Year 2017)
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| Budget Amount *help |
¥40,690,000 (Direct Cost: ¥31,300,000、Indirect Cost: ¥9,390,000)
Fiscal Year 2017: ¥10,140,000 (Direct Cost: ¥7,800,000、Indirect Cost: ¥2,340,000)
Fiscal Year 2016: ¥10,140,000 (Direct Cost: ¥7,800,000、Indirect Cost: ¥2,340,000)
Fiscal Year 2015: ¥20,410,000 (Direct Cost: ¥15,700,000、Indirect Cost: ¥4,710,000)
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| Keywords | 構造生物学 / 生物物理 / 細菌 / 結晶構造解析 / 電子顕微鏡 / 蛋白質輸送 |
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| Outline of Final Research Achievements |
Type III secretion system (T3SS) is one of the bacterial protein transporters used to deliver virulence proteins directly into their eukaryotic host cells for infection. To elucidate the molecular mechanism of the type III secretion, we investigated the flagellar T3SS, which is used for construction of the bacterial flagellum and is the most well-studied T3SS, by X-ray crystallography, electron microscopy, atomic force microscopy and inverted membrane vesicle assay techniques. We solved the structure of the export ATPase complex and found its novel roles on T3SS export. The structure of an export chaperone was also determined and the regulation mechanism of the secretion order was revealed. In addition, we proposed novel mechanistic models on the flagellar protein export, such as the mechanism of the export substrate switching, the assembly mechanism of the export gate complex and regulation of protein export by the interaction between the export substrates.
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Report
(4 results)
Research Products
(59 results)
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[Journal Article] Rearrangements of α-helical structures of FlgN chaperone control the binding affinity for its cognate substrates during flagellar type III export.2016
Author(s)
Kinoshita, M., Nakanishi, Y., Furukawa, Y., Namba, K., Imada, K., Minamino, T.
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Journal Title
Mol. Microbiol.
Volume: 101
Issue: 4
Pages: 656-670
DOI
Related Report
Peer Reviewed / Acknowledgement Compliant
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[Presentation] 蛍光ラベルした細菌べん毛蛋白質のin vitro輸送測定系を用いた検出.2016
Author(s)
戸野侃, 寺島浩行, 巽千夏, 川本晃大, 田端和仁, 上野博史, 松田知己, 永井健治, 野地博行, 難波啓一, 南野徹, 今田勝巳.
Organizer
日本生体エネルギー研究会第42回討論会
Place of Presentation
名古屋工業大学
Related Report
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